摘要
用荧光光谱、紫外-可见吸收光谱和圆二色谱等光谱方法研究了生理条件下硫堇(TH)与人血清白蛋白(HSA)的作用机理。测得不同温度下,硫堇与人血清白蛋白的结合常数和结合位点数,确定硫堇对人血清白蛋白荧光的猝灭是静态猝灭过程,并依据Forster无辐射能量转移理论获得了TH与HSA的结合距离4.604 nm,热力学参数ΔH=-9.024 kJ/mol,ΔS=40.63 J.mol-1.K-1,表明TH与HSA主要为静电力相互作用,同步荧光光谱和圆二色谱显示了TH对HSA的二级结构构象产生影响。
The binding reaction between thionine（TH） and human serum albumin（HSA） in physiological conditions was studied by fluorescence spectroscopy in combination with circular dichroism spectroscopy and UV-Vis absorbance spectrometry.The apparent binding constant and the number of binding sites at different temperatures were calculated and the quenching mechanism was suggested as static quenching.The distance between HSA and TH was estimated to be 4.604 nm using the Foster′s equation on the basis of fluorescence energy transfer.The thermodynamic parameters ΔH and ΔS for the HSA-TH system were calculated to be-9.024 kJ/mol and 40.63 J·mol^-1·K^-1hich indicated that electrostatic interactions played a major role in the interaction.Synchronous fluorescence spectra and circular dichroism spectra of HSA in the presence of thionine indicated that the conformations of human serum albumin had been changed.
出处
《化学试剂》
CAS
CSCD
北大核心
2009年第3期180-182,193,共4页
Chemical Reagents
关键词
荧光光谱
圆二色谱
硫堇
人血清白蛋白
fluorescence spectroscopy
circular dichroism spectroscopy
thionine
human serum albumin
